H2AC1

Histone H2A type 1 (H2AC1), also termed H2A.1 or H2A/I, is a core component of nucleosomes responsible for DNA packaging and chromatin organization. As part of the H2A-H2B dimer, it stabilizes DNA-histone interactions and regulates transcriptional accessibility through post-translational modifications such as ubiquitination and phosphorylation. These modifications mediate DNA repair via homologous recombination and non-homologous end joining, as well as epigenetic regulation of gene silencing. Dysregulation of H2AC1 is implicated in chromatin remodeling defects, influencing genomic instability in cancers like leukemia and lymphoma.
H2AC1 interacts with signaling pathways including ATM/ATR-mediated DNA damage response and Polycomb repressive complexes (PRC1/PRC2) for transcriptional repression. Aberrant H2A variants are linked to autoimmune disorders such as systemic lupus erythematosus, where anti-histone antibodies target modified H2A epitopes. Current drug development focuses on modulating histone modifications, with HDAC inhibitors (e.g., vorinostat) and EZH2 inhibitors (tazemetostat) showing clinical efficacy in H2A-related malignancies. Novel therapies targeting H2A ubiquitination (e.g., USP7 inhibitors) are under preclinical evaluation for synthetic lethality approaches.

Popular Product:

Recombinant Human Histone H2A type 1-A (H2AC1)